Back to Search
Start Over
Structural insight into the substrate specificity of DNA Polymerase μ
- Source :
- Nature Structural & Molecular Biology. 14:45-53
- Publication Year :
- 2006
- Publisher :
- Springer Science and Business Media LLC, 2006.
-
Abstract
- DNA polymerase mu (Pol mu) is a family X enzyme with unique substrate specificity that contributes to its specialized role in nonhomologous DNA end joining (NHEJ). To investigate Pol mu's unusual substrate specificity, we describe the 2.4 A crystal structure of the polymerase domain of murine Pol mu bound to gapped DNA with a correct dNTP at the active site. This structure reveals substrate interactions with side chains in Pol mu that differ from other family X members. For example, a single amino acid substitution, H329A, has little effect on template-dependent synthesis by Pol mu from a paired primer terminus, but it reduces both template-independent and template-dependent synthesis during NHEJ of intermediates whose 3' ends lack complementary template strand nucleotides. These results provide insight into the substrate specificity and differing functions of four closely related mammalian family X DNA polymerases.
- Subjects :
- Models, Molecular
DNA Repair
DNA polymerase
Stereochemistry
DNA polymerase II
Molecular Sequence Data
DNA-Directed DNA Polymerase
Crystallography, X-Ray
DNA polymerase delta
Substrate Specificity
Mice
Structural Biology
Animals
Thymine Nucleotides
Amino Acid Sequence
Molecular Biology
Polymerase
Binding Sites
DNA clamp
biology
DNA replication
DNA
Processivity
Molecular biology
Protein Structure, Tertiary
DNA-Binding Proteins
Amino Acid Substitution
biology.protein
Sequence Alignment
DNA polymerase mu
Dideoxynucleotides
Subjects
Details
- ISSN :
- 15459985 and 15459993
- Volume :
- 14
- Database :
- OpenAIRE
- Journal :
- Nature Structural & Molecular Biology
- Accession number :
- edsair.doi.dedup.....2b35e270e75ccd0777d6f7abf0b02833